{
    "uniprot_canonical_ac": "P0DTC2-1",
    "uniprot_ac": "P0DTC2",
    "uniprot_id": "SPIKE_SARS2",
    "mass": {
        "chemical_mass": 141178.0,
        "monoisotopic_mass": 141178.0
    },
    "refseq": {
        "ac": "YP_009724390",
        "name": "surface glycoprotein",
        "summary": "",
        "url": "https://www.ncbi.nlm.nih.gov/protein/YP_009724390"
    },
    "gene_names": [
        {
            "name": "S",
            "resource": "UniProtKB",
            "type": "recommended",
            "url": "https://www.uniprot.org/uniprot/P0DTC2",
            "id": "P0DTC2"
        },
        {
            "name": "2",
            "resource": "UniProtKB",
            "type": "synonym",
            "url": "https://www.uniprot.org/uniprot/P0DTC2",
            "id": "P0DTC2"
        }
    ],
    "protein_names": [
        {
            "name": "Spike glycoprotein",
            "resource": "UniProtKB",
            "type": "recommended",
            "url": "https://www.uniprot.org/uniprotkb/P0DTC2/entry#names_and_taxonomy",
            "id": "P0DTC2"
        },
        {
            "name": "E2",
            "resource": "UniProtKB",
            "type": "synonym",
            "url": "https://www.uniprot.org/uniprotkb/P0DTC2/entry#names_and_taxonomy",
            "id": "P0DTC2"
        },
        {
            "name": "Peplomer protein",
            "resource": "UniProtKB",
            "type": "synonym",
            "url": "https://www.uniprot.org/uniprotkb/P0DTC2/entry#names_and_taxonomy",
            "id": "P0DTC2"
        },
        {
            "name": "S glycoprotein",
            "resource": "UniProtKB",
            "type": "synonym",
            "url": "https://www.uniprot.org/uniprotkb/P0DTC2/entry#names_and_taxonomy",
            "id": "P0DTC2"
        },
        {
            "name": "surface glycoprotein",
            "resource": "RefSeq",
            "type": "synonym",
            "url": "https://www.ncbi.nlm.nih.gov/protein/YP_009724390",
            "id": "YP_009724390"
        }
    ],
    "function": [
        {
            "annotation": "Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. The major receptor is host ACE2 (PubMed:32142651, PubMed:32155444, PubMed:33607086). When S2/S2' has been cleaved, binding to the receptor triggers direct fusion at the cell membrane (PubMed:34561887). When S2/S2' has not been cleaved, binding to the receptor results in internalization of the virus by endocytosis leading to fusion of the virion membrane with the host endosomal membrane (PubMed:32075877, PubMed:32221306). Alternatively, may use NRP1/NRP2 (PubMed:33082294, PubMed:33082293) and integrin as entry receptors (PubMed:35150743). The use of NRP1/NRP2 receptors may explain the tropism of the virus in human olfactory epithelial cells, which express these molecules at high levels but ACE2 at low levels (PubMed:33082293). The stalk domain of S contains three hinges, giving the head unexpected orientational freedom (PubMed:32817270).",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2#function"
                },
                {
                    "database": "PubMed",
                    "id": "32075877",
                    "url": "https://glygen.org/publication/PubMed/32075877"
                },
                {
                    "database": "HAMAP",
                    "id": "MF_04099",
                    "url": "https://hamap.expasy.org/signature/MF_04099"
                },
                {
                    "database": "PubMed",
                    "id": "32155444",
                    "url": "https://glygen.org/publication/PubMed/32155444"
                },
                {
                    "database": "PubMed",
                    "id": "32142651",
                    "url": "https://glygen.org/publication/PubMed/32142651"
                },
                {
                    "database": "PubMed",
                    "id": "32221306",
                    "url": "https://glygen.org/publication/PubMed/32221306"
                },
                {
                    "database": "PubMed",
                    "id": "34561887",
                    "url": "https://glygen.org/publication/PubMed/34561887"
                },
                {
                    "database": "PubMed",
                    "id": "35150743",
                    "url": "https://glygen.org/publication/PubMed/35150743"
                },
                {
                    "database": "PubMed",
                    "id": "33082294",
                    "url": "https://glygen.org/publication/PubMed/33082294"
                },
                {
                    "database": "PubMed",
                    "id": "33082293",
                    "url": "https://glygen.org/publication/PubMed/33082293"
                },
                {
                    "database": "PubMed",
                    "id": "32817270",
                    "url": "https://glygen.org/publication/PubMed/32817270"
                }
            ]
        },
        {
            "annotation": "Precursor of the fusion protein processed in the biosynthesis of the S protein and the formation of virus particle. Mediates fusion of the virion and cellular membranes by functioning as a class I viral fusion protein. Contains two viral fusion peptides that are unmasked after cleavage. The S2/S2' cleavage occurs during virus entry at the cell membrane by host TMPRSS2 (PubMed:32142651) or during endocytosis by host CSTL (PubMed:32703818, PubMed:34159616). In either case, this triggers an extensive and irreversible conformational change leading to fusion of the viral envelope with the cellular cytoplasmic membrane, releasing viral genomic RNA into the host cell cytoplasm (PubMed:34561887). Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of the viral and target cell membranes, the coiled coil regions (heptad repeats) adopt a trimer-of-hairpins structure and position the fusion peptide in close proximity to the C-terminal region of the ectodomain. Formation of this structure appears to promote apposition and subsequent fusion of viral and target cell membranes.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2#function"
                },
                {
                    "database": "HAMAP",
                    "id": "MF_04099",
                    "url": "https://hamap.expasy.org/signature/MF_04099"
                },
                {
                    "database": "PubMed",
                    "id": "34561887",
                    "url": "https://glygen.org/publication/PubMed/34561887"
                },
                {
                    "database": "PubMed",
                    "id": "32703818",
                    "url": "https://glygen.org/publication/PubMed/32703818"
                },
                {
                    "database": "PubMed",
                    "id": "34159616",
                    "url": "https://glygen.org/publication/PubMed/34159616"
                }
            ]
        },
        {
            "annotation": "Subunit of the fusion protein that is processed upon entry into the host cell. Mediates fusion of the virion and cellular membranes by functioning as a class I viral fusion protein. Contains a viral fusion peptide that is unmasked after S2 cleavage. This cleavage can occur at the cell membrane by host TMPRSS2 or during endocytosis by host CSTL (PubMed:32703818, PubMed:34159616). In either case, this triggers an extensive and irreversible conformational change that leads to fusion of the viral envelope with the cellular cytoplasmic membrane, releasing viral genomic RNA into the host cell cytoplasm (PubMed:34561887). Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of the viral and target cell membranes, the coiled coil regions (heptad repeats) adopt a trimer-of-hairpins structure and position the fusion peptide in close proximity to the C-terminal region of the ectodomain. Formation of this structure appears to promote apposition and subsequent fusion of viral and target cell membranes.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2#function"
                },
                {
                    "database": "HAMAP",
                    "id": "MF_04099",
                    "url": "https://hamap.expasy.org/signature/MF_04099"
                },
                {
                    "database": "PubMed",
                    "id": "34561887",
                    "url": "https://glygen.org/publication/PubMed/34561887"
                },
                {
                    "database": "PubMed",
                    "id": "32703818",
                    "url": "https://glygen.org/publication/PubMed/32703818"
                },
                {
                    "database": "PubMed",
                    "id": "34159616",
                    "url": "https://glygen.org/publication/PubMed/34159616"
                }
            ]
        }
    ],
    "disease": [],
    "snv": [],
    "mutagenesis": [
        {
            "start_pos": 121,
            "end_pos": 121,
            "sequence_org": "N",
            "sequence_mut": "Q",
            "comment": "Partial loss of biliverdin affinity.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "33888467",
                    "url": "https://glygen.org/publication/PubMed/33888467"
                }
            ]
        },
        {
            "start_pos": 1269,
            "end_pos": 1269,
            "sequence_org": "K",
            "sequence_mut": "A",
            "comment": "Complete loss of COPI binding and increase in cell fusion.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34504087",
                    "url": "https://glygen.org/publication/PubMed/34504087"
                }
            ]
        },
        {
            "start_pos": 1271,
            "end_pos": 1271,
            "sequence_org": "H",
            "sequence_mut": "K",
            "comment": "Improved COPI binding, reduced cell fusion and reduced levels of S1/S2 cleavage.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34504087",
                    "url": "https://glygen.org/publication/PubMed/34504087"
                }
            ]
        },
        {
            "start_pos": 190,
            "end_pos": 190,
            "sequence_org": "R",
            "sequence_mut": "K",
            "comment": "Partial loss of biliverdin affinity.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "33888467",
                    "url": "https://glygen.org/publication/PubMed/33888467"
                }
            ]
        },
        {
            "start_pos": 234,
            "end_pos": 234,
            "sequence_org": "N",
            "sequence_mut": "Q",
            "comment": "Increased resistance to neutralizing antibodies.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32730807",
                    "url": "https://glygen.org/publication/PubMed/32730807"
                }
            ]
        },
        {
            "start_pos": 331,
            "end_pos": 331,
            "sequence_org": "N",
            "sequence_mut": "Q",
            "comment": "Reduced viral infectivity.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32730807",
                    "url": "https://glygen.org/publication/PubMed/32730807"
                }
            ]
        },
        {
            "start_pos": 343,
            "end_pos": 343,
            "sequence_org": "N",
            "sequence_mut": "Q",
            "comment": "Reduced viral infectivity.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32730807",
                    "url": "https://glygen.org/publication/PubMed/32730807"
                }
            ]
        },
        {
            "start_pos": 452,
            "end_pos": 452,
            "sequence_org": "L",
            "sequence_mut": "R",
            "comment": "Increased resistance to neutralizing antibodies. Decreases HLA binding to NF9 epitope. Increased binding affinity to human ACE2.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32730807",
                    "url": "https://glygen.org/publication/PubMed/32730807"
                },
                {
                    "database": "PubMed",
                    "id": "34171266",
                    "url": "https://glygen.org/publication/PubMed/34171266"
                }
            ]
        },
        {
            "start_pos": 453,
            "end_pos": 453,
            "sequence_org": "Y",
            "sequence_mut": "F",
            "comment": "Decreased HLA binding to NF9 epitope. Increased binding affinity to human ACE2.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34171266",
                    "url": "https://glygen.org/publication/PubMed/34171266"
                }
            ]
        },
        {
            "start_pos": 475,
            "end_pos": 475,
            "sequence_org": "A",
            "sequence_mut": "V",
            "comment": "Increased resistance to neutralizing antibodies.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32730807",
                    "url": "https://glygen.org/publication/PubMed/32730807"
                }
            ]
        },
        {
            "start_pos": 483,
            "end_pos": 483,
            "sequence_org": "V",
            "sequence_mut": "A",
            "comment": "Increased resistance to neutralizing antibodies.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32730807",
                    "url": "https://glygen.org/publication/PubMed/32730807"
                }
            ]
        },
        {
            "start_pos": 484,
            "end_pos": 484,
            "sequence_org": "E",
            "sequence_mut": "D",
            "comment": "Increased replication in human TMEM106B overexpressing cells.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "37421949",
                    "url": "https://glygen.org/publication/PubMed/37421949"
                }
            ]
        },
        {
            "start_pos": 490,
            "end_pos": 490,
            "sequence_org": "F",
            "sequence_mut": "L",
            "comment": "Increased resistance to neutralizing antibodies and human covalescent sera neutralization.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32730807",
                    "url": "https://glygen.org/publication/PubMed/32730807"
                }
            ]
        },
        {
            "start_pos": 493,
            "end_pos": 493,
            "sequence_org": "Q",
            "sequence_mut": "N",
            "comment": "Reduced host ACE2-binding affinity in vitro.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32225175",
                    "url": "https://glygen.org/publication/PubMed/32225175"
                }
            ]
        },
        {
            "start_pos": 493,
            "end_pos": 493,
            "sequence_org": "Q",
            "sequence_mut": "Y",
            "comment": "Reduced host ACE2-binding affinity in vitro.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32225175",
                    "url": "https://glygen.org/publication/PubMed/32225175"
                }
            ]
        },
        {
            "start_pos": 501,
            "end_pos": 501,
            "sequence_org": "N",
            "sequence_mut": "T",
            "comment": "Reduced host ACE2-binding affinity in vitro.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32225175",
                    "url": "https://glygen.org/publication/PubMed/32225175"
                }
            ]
        },
        {
            "start_pos": 501,
            "end_pos": 501,
            "sequence_org": "N",
            "sequence_mut": "Y",
            "comment": "Increased binding affinity to human ACE2.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34171266",
                    "url": "https://glygen.org/publication/PubMed/34171266"
                }
            ]
        },
        {
            "start_pos": 519,
            "end_pos": 519,
            "sequence_org": "H",
            "sequence_mut": "P",
            "comment": "Increased resistance to human covalescent sera neutralization.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32730807",
                    "url": "https://glygen.org/publication/PubMed/32730807"
                }
            ]
        },
        {
            "start_pos": 614,
            "end_pos": 614,
            "sequence_org": "D",
            "sequence_mut": "G",
            "comment": "Increase of pseudotyped VSV particle production ex vivo. Increase of viral load in hamster upper respiratory tract. Produces more infectious particles when cultured in primary human epithelial cells; increases replication and transmissibility in hamsters and ferrets.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32697968",
                    "url": "https://glygen.org/publication/PubMed/32697968"
                },
                {
                    "database": "PubMed",
                    "id": "33636719",
                    "url": "https://glygen.org/publication/PubMed/33636719"
                },
                {
                    "database": "PubMed",
                    "id": "33106671",
                    "url": "https://glygen.org/publication/PubMed/33106671"
                }
            ]
        },
        {
            "start_pos": 673,
            "end_pos": 673,
            "sequence_org": "S",
            "sequence_mut": "A",
            "comment": "No effect on O-glycosylation by host GALNT1.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34732583",
                    "url": "https://glygen.org/publication/PubMed/34732583"
                }
            ]
        },
        {
            "start_pos": 676,
            "end_pos": 676,
            "sequence_org": "T",
            "sequence_mut": "A",
            "comment": "Partial loss of O-glycosylation by host GALNT1.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34732583",
                    "url": "https://glygen.org/publication/PubMed/34732583"
                }
            ]
        },
        {
            "start_pos": 678,
            "end_pos": 678,
            "sequence_org": "T",
            "sequence_mut": "A",
            "comment": "Complete loss of O-glycosylation by host GALNT1.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34732583",
                    "url": "https://glygen.org/publication/PubMed/34732583"
                }
            ]
        },
        {
            "start_pos": 679,
            "end_pos": 684,
            "sequence_org": "NSPRRA",
            "sequence_mut": "IL",
            "comment": "About 50% stronger entry efficiency in Vero E6 cells while 30% weaker entry efficiency in hACE2-expressing BHK cells.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32155444",
                    "url": "https://glygen.org/publication/PubMed/32155444"
                }
            ]
        },
        {
            "start_pos": 680,
            "end_pos": 680,
            "sequence_org": "S",
            "sequence_mut": "A",
            "comment": "No effect on O-glycosylation by host GALNT1.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34732583",
                    "url": "https://glygen.org/publication/PubMed/34732583"
                }
            ]
        },
        {
            "start_pos": 681,
            "end_pos": 681,
            "sequence_org": "P",
            "sequence_mut": "A",
            "comment": "Complete loss of O-glycosylation by host GALNT1.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34732583",
                    "url": "https://glygen.org/publication/PubMed/34732583"
                }
            ]
        },
        {
            "start_pos": 681,
            "end_pos": 681,
            "sequence_org": "P",
            "sequence_mut": "H",
            "comment": "Complete loss of O-glycosylation by host GALNT1.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34732583",
                    "url": "https://glygen.org/publication/PubMed/34732583"
                }
            ]
        },
        {
            "start_pos": 681,
            "end_pos": 681,
            "sequence_org": "P",
            "sequence_mut": "R",
            "comment": "Complete loss of O-glycosylation by host GALNT1.",
            "evidence": [
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            "categories": [
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            ]
        },
        {
            "id": "PF19209",
            "url": "https://www.ebi.ac.uk/interpro/entry/pfam/PF19209",
            "database": "Pfam",
            "categories": [
                "Protein Classification"
            ]
        },
        {
            "id": "YP_009724390",
            "url": "https://www.ncbi.nlm.nih.gov/protein/YP_009724390",
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            ]
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            ]
        },
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            "id": "P0DTC2-1",
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        },
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            "id": "P0DTC2",
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        }
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        "header": "sp|P0DTC2-1|SPIKE_SARS2 Isoform 1 of Spike glycoprotein  OS=Severe acute respiratory syndrome coronavirus 2 OX=2697049 GN=S PE=1 SV=1 CANONICAL=P0DTC2-1"
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                    {
                        "name": "host cell endoplasmic reticulum-Golgi intermediate compartment membrane",
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                                "id": "P0DTC2",
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                    },
                    {
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                        "evidence": [
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                        ],
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                    {
                        "name": "host extracellular space",
                        "id": "GO:0043655",
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                                "id": "P0DTC2",
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                            }
                        ],
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                    }
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            },
            {
                "name": "Molecular Function",
                "total": 4,
                "go_terms": [
                    {
                        "name": "identical protein binding",
                        "id": "GO:0042802",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042802",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "receptor ligand activity",
                        "id": "GO:0048018",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048018",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "host cell surface receptor binding",
                        "id": "GO:0046789",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046789",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "structural constituent of virion",
                        "id": "GO:0039660",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039660",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    }
                ]
            },
            {
                "name": "Biological Process",
                "total": 11,
                "go_terms": [
                    {
                        "name": "positive regulation of viral entry into host cell",
                        "id": "GO:0046598",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046598",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "receptor-mediated virion attachment to host cell",
                        "id": "GO:0046813",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046813",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "membrane fusion",
                        "id": "GO:0061025",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0061025",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "viral translation",
                        "id": "GO:0019081",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019081",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "fusion of virus membrane with host plasma membrane",
                        "id": "GO:0019064",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019064",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "virion attachment to host cell",
                        "id": "GO:0019062",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019062",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "suppression by virus of host tetherin activity",
                        "id": "GO:0039587",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039587",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "endocytosis involved in viral entry into host cell",
                        "id": "GO:0075509",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0075509",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "fusion of virus membrane with host endosome membrane",
                        "id": "GO:0039654",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0039654",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "entry receptor-mediated virion attachment to host cell",
                        "id": "GO:0098670",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0098670",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    },
                    {
                        "name": "symbiont-mediated suppression of host innate immune response",
                        "id": "GO:0052170",
                        "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0052170",
                        "evidence": [
                            {
                                "database": "UniProtKB",
                                "id": "P0DTC2",
                                "url": "https://www.uniprot.org/uniprot/P0DTC2"
                            }
                        ],
                        "pmid": ""
                    }
                ]
            }
        ]
    },
    "pro_annotation": [],
    "site_annotation": [
        {
            "start_pos": 1074,
            "end_pos": 1076,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 1098,
            "end_pos": 1100,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 1134,
            "end_pos": 1136,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 1158,
            "end_pos": 1160,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 1173,
            "end_pos": 1175,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 1194,
            "end_pos": 1196,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 122,
            "end_pos": 124,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 149,
            "end_pos": 151,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 165,
            "end_pos": 167,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 17,
            "end_pos": 19,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 234,
            "end_pos": 236,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 282,
            "end_pos": 284,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 331,
            "end_pos": 333,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 343,
            "end_pos": 345,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 603,
            "end_pos": 605,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 616,
            "end_pos": 618,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 61,
            "end_pos": 63,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 657,
            "end_pos": 659,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 709,
            "end_pos": 711,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 717,
            "end_pos": 719,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 74,
            "end_pos": 76,
            "annotation": "n_glycosylation_sequon"
        },
        {
            "start_pos": 801,
            "end_pos": 803,
            "annotation": "n_glycosylation_sequon"
        }
    ],
    "ptm_annotation": [
        {
            "annotation": "Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138). Highly glycosylated by host both on S1 and S2 subunits, occluding many regions across the surface of the protein (PubMed:32363391, PubMed:32366695, PubMed:32929138). Approximately 40% of the protein surface is shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain (PubMed:32929138).",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32929138",
                    "url": "https://glygen.org/publication/PubMed/32929138"
                },
                {
                    "database": "PubMed",
                    "id": "32155444",
                    "url": "https://glygen.org/publication/PubMed/32155444"
                },
                {
                    "database": "PubMed",
                    "id": "32366695",
                    "url": "https://glygen.org/publication/PubMed/32366695"
                },
                {
                    "database": "PubMed",
                    "id": "32075877",
                    "url": "https://glygen.org/publication/PubMed/32075877"
                },
                {
                    "database": "PubMed",
                    "id": "32363391",
                    "url": "https://glygen.org/publication/PubMed/32363391"
                }
            ]
        },
        {
            "annotation": "O-glycosylated by host GALNT1 at the end of S1. This could reduce the efficiency of S1/S2 cleavage.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34732583",
                    "url": "https://glygen.org/publication/PubMed/34732583"
                }
            ]
        },
        {
            "annotation": "Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32155444, PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835).",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "32155444",
                    "url": "https://glygen.org/publication/PubMed/32155444"
                },
                {
                    "database": "PubMed",
                    "id": "32142651",
                    "url": "https://glygen.org/publication/PubMed/32142651"
                },
                {
                    "database": "PubMed",
                    "id": "32362314",
                    "url": "https://glygen.org/publication/PubMed/32362314"
                },
                {
                    "database": "PubMed",
                    "id": "33465165",
                    "url": "https://glygen.org/publication/PubMed/33465165"
                },
                {
                    "database": "PubMed",
                    "id": "34561887",
                    "url": "https://glygen.org/publication/PubMed/34561887"
                },
                {
                    "database": "PubMed",
                    "id": "32703818",
                    "url": "https://glygen.org/publication/PubMed/32703818"
                },
                {
                    "database": "PubMed",
                    "id": "33417835",
                    "url": "https://glygen.org/publication/PubMed/33417835"
                },
                {
                    "database": "PubMed",
                    "id": "34159616",
                    "url": "https://glygen.org/publication/PubMed/34159616"
                },
                {
                    "database": "PubMed",
                    "id": "32221306",
                    "url": "https://glygen.org/publication/PubMed/32221306"
                }
            ]
        },
        {
            "annotation": "The cytoplasmic Cys-rich domain is palmitoylated. Palmitoylated spike proteins drive the formation of localized ordered cholesterol and sphingo-lipid-rich lipid nanodomains in the early Golgi, where viral budding occurs.",
            "evidence": [
                {
                    "database": "UniProtKB",
                    "id": "P0DTC2",
                    "url": "https://www.uniprot.org/uniprot/P0DTC2"
                },
                {
                    "database": "PubMed",
                    "id": "34599882",
                    "url": "https://glygen.org/publication/PubMed/34599882"
                }
            ]
        }
    ],
    "interactions": [],
    "reactions": [],
    "reaction_participants": [],
    "reaction_enzymes": [],
    "biomarkers": [],
    "structures": [],
    "synthesized_glycans": [],
    "enzyme_annotation": [],
    "cluster_types": [
        {
            "name": "homologset.uniref",
            "label": "UniRef Homologs"
        }
    ],
    "sequence_features": {
        "n_linked_sites": [
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            74,
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            234,
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            331,
            343,
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            657,
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            709,
            717,
            801,
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            1098,
            1134,
            1158,
            1173,
            1194
        ],
        "o_linked_sites": [
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            71,
            73,
            76,
            94,
            95,
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            124,
            151,
            167,
            236,
            315,
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            417,
            478,
            489,
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            500,
            505,
            523,
            618,
            676,
            678,
            803,
            1076,
            1077,
            1097,
            1100
        ],
        "snv_sites": [],
        "glycation_sites": [],
        "phosphorylation_sites": [],
        "sequon_annotation_sites": [
            {
                "start_pos": 1074,
                "end_pos": 1076
            },
            {
                "start_pos": 1098,
                "end_pos": 1100
            },
            {
                "start_pos": 1134,
                "end_pos": 1136
            },
            {
                "start_pos": 1158,
                "end_pos": 1160
            },
            {
                "start_pos": 1173,
                "end_pos": 1175
            },
            {
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                "end_pos": 1196
            },
            {
                "start_pos": 122,
                "end_pos": 124
            },
            {
                "start_pos": 149,
                "end_pos": 151
            },
            {
                "start_pos": 165,
                "end_pos": 167
            },
            {
                "start_pos": 17,
                "end_pos": 19
            },
            {
                "start_pos": 234,
                "end_pos": 236
            },
            {
                "start_pos": 282,
                "end_pos": 284
            },
            {
                "start_pos": 331,
                "end_pos": 333
            },
            {
                "start_pos": 343,
                "end_pos": 345
            },
            {
                "start_pos": 603,
                "end_pos": 605
            },
            {
                "start_pos": 616,
                "end_pos": 618
            },
            {
                "start_pos": 61,
                "end_pos": 63
            },
            {
                "start_pos": 657,
                "end_pos": 659
            },
            {
                "start_pos": 709,
                "end_pos": 711
            },
            {
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                "end_pos": 719
            },
            {
                "start_pos": 74,
                "end_pos": 76
            },
            {
                "start_pos": 801,
                "end_pos": 803
            }
        ]
    },
    "section_stats": [
        {
            "table_id": "glycosylation",
            "table_stats": [
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                    "field": "total",
                    "count": 2733
                },
                {
                    "field": "total_sites",
                    "count": 59
                },
                {
                    "field": "n_linked_sites",
                    "count": 25
                },
                {
                    "field": "o_linked_sites",
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                },
                {
                    "field": "n_linked_glycan_sites",
                    "count": 22
                },
                {
                    "field": "o_linked_glycan_sites",
                    "count": 27
                },
                {
                    "field": "n_linked_glycans",
                    "count": 2091
                },
                {
                    "field": "o_linked_glycans",
                    "count": 72
                },
                {
                    "field": "exact_sites",
                    "count": 58
                },
                {
                    "field": "exact_n_linked_sites",
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                },
                {
                    "field": "exact_n_linked_glycan_sites",
                    "count": 22
                },
                {
                    "field": "exact_n_linked_glycans",
                    "count": 2091
                },
                {
                    "field": "exact_n_linked;o_linked_sites",
                    "count": 22
                },
                {
                    "field": "exact_n_linked;o_linked_glycan_sites",
                    "count": 22
                },
                {
                    "field": "exact_n_linked;o_linked_glycans",
                    "count": 507
                },
                {
                    "field": "exact_o_linked_sites",
                    "count": 33
                },
                {
                    "field": "exact_o_linked_glycan_sites",
                    "count": 27
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                {
                    "field": "exact_o_linked_glycans",
                    "count": 72
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                {
                    "field": "fuzzy_sites",
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                },
                {
                    "field": "fuzzy_n_linked_sites",
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                {
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                {
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                "prediction_tool",
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        {
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